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Título

AMP-activated protein kinase: structure and regulation.

Autor Sanz, Pascual
Palabras clave AMP-activated protein kinase
Snf1
LKB1
CaMKK
Phosphatase
Fecha de publicación oct-2008
EditorBentham Science Publishers
Citación Current Protein and Peptide Science 9(5):478-92. (2008)
ResumenMammalian AMP-activated protein kinase (AMPK) is a serine/threonine protein kinase that acts as a sensor of cellular energy status. It is activated by a large variety of cellular stresses that increase cellular AMP and decrease ATP levels and also by physiological stimuli, such as muscle contraction, or by hormones such as leptin and adiponectin. AMPK modulates multiple metabolic pathways. As a result, it has become a target for the development of new drugs for the treatment of type II diabetes, obesity or even cancer. In fact, it has been recently reported that drugs used in the treatment of diabetes, such as metformin and thiazolidinediones (TZDs), exert their beneficial effects through the activation of AMPK. AMPK is a heterotrimeric complex composed of a catalytic subunit (AMPK-) and two regulatory subunits (AMPK- and AMPK-). Functional orthologues of this kinase complex are found throughout eukaryotic kingdom, from yeast to humans, indicating that the function of this complex is evolutionarily conserved. This review summarizes the recent studies on the structure and regulation of the AMPK heterotrimeric complex.
Descripción 15 páginas, 5 figuras, 3 tablas
Versión del editorhttp://dx.doi.org/10.2174/138920308785915254
URI http://hdl.handle.net/10261/112095
DOI10.2174/138920308785915254
ISSN1389-2037
E-ISSN1875-5550
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